1bhg

From Proteopedia

---

Revision as of 14:03, 12 November 2007

proteopedia linkproteopedia link

spinqualitylabelsall models 1bhg, resolution 2.53Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HUMAN BETA-GLUCURONIDASE AT 2.6 A RESOLUTION

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

The X-ray structure of the homotetrameric lysosomal acid hydrolase, human, beta-glucuronidase (332,000 Mr), has been determined at 2.6 A resolution., The tetramer has approximate dihedral symmetry and each promoter consists, of three structural domains with topologies similar to a jelly roll, barrel, an immunoglobulin constant domain and a TIM barrel respectively., Residues 179-204 form a beta-hairpin motif similar to the putative, lysosomal targeting motif of cathepsin D, supporting the view that, lysosomal targeting has a structural basis. The active site of the enzyme, is formed from a large cleft at the interface of two monomers. Residues, Glu 451 and Glu 540 are proposed to be important for catalysis. The, structure establishes a framework for understanding mutations that lead to, the human genetic disease mucopolysaccharidosis VII, and for using the, enzyme in anti-cancer therapy.

Disease

Known disease associated with this structure: Mucopolysaccharidosis VII OMIM:[253220]

About this Structure

1BHG is a Single protein structure of sequence from Homo sapiens. Active as Beta-glucuronidase, with EC number 3.2.1.31 Full crystallographic information is available from OCA.

Reference

Structure of human beta-glucuronidase reveals candidate lysosomal targeting and active-site motifs., Jain S, Drendel WB, Chen ZW, Mathews FS, Sly WS, Grubb JH, Nat Struct Biol. 1996 Apr;3(4):375-81. PMID:8599764

Page seeded by OCA on Mon Nov 12 16:09:45 2007